Lipase Engineering Database

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Lipase Engineering Database

metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:29.628197

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Lipase_Engineering_Database

metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:29.628197

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Other names: Lipase_Engineering_Database

The Lipase Engineering Database (http://www.led.uni-stuttgart.de) integrates information on sequence, structure, and function of lipases, esterases, and related proteins. Sequence data on 806 protein entries are assigned to 38 homologous families, which are grouped into 16 superfamilies with no global sequence similarity among each other. For each family, multisequence alignments are provided with functionally relevant residues annotated. Pre-calculated phylogenetic trees allow navigation inside superfamilies. Experimental structures of 45 proteins are superposed and consistently annotated. The Lipase Engineering Database has been applied to systematically analyze sequence-structure-function relationships of this vast and diverse enzyme class. It is a useful tool to identify functionally relevant residues apart from the active site residues, and to design mutants with desired substrate specificity.

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The modular structure of α/β-hydrolases
PMID: 31545554

metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:29.628197

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• The modular structure of α/β-hydrolases PubMed citations: 7.

  7 articles citing: The modular structure of α/β-hydrolases

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  Gallic Acid as a Non-Selective Inhibitor of α/β-Hydrolase Fold Enzymes Involved in the Inflammatory Process: The Two Sides of the Same Coin. PMID:35214100

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  Structure-function relationship between soluble epoxide hydrolases structure and their tunnel network. PMID:35024092

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  Structure and evolutionary trace-assisted screening of a residue swapping the substrate ambiguity and chiral specificity in an esterase. PMID:33995922

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  Structure and Dynamics of an Archeal Monoglyceride Lipase from Palaeococcus ferrophilus as Revealed by Crystallography and In Silico Analysis. PMID:33916727

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  An extracellular lipase from Amycolatopsis mediterannei is a cutinase with plastic degrading activity. PMID:33598102

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  Cold Active Lipases: Biocatalytic Tools for Greener Technology. PMID:33544363

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  Molecular and Structural Characterizations of Lipases from Chlorella by Functional Genomics. PMID:33525674

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protein sequence databases

metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

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databases of individual protein families

metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

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protein folds and structural domains

metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:29.628197

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small molecules

metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:29.628197

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protein folding, stability and design

metasource: bio.tools
version: extracted_at: 2022-11-04T11:29:29.628197

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protein sequence protein family protein folds and structural domains small molecule protein folding, stability and design